Structural basis of ribosomal RNA transcription regulation.
| Autor: | Shin Y; Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, 16802, USA., Qayyum MZ; Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, 16802, USA., Pupov D; Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, 123182, Russia., Esyunina D; Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, 123182, Russia., Kulbachinskiy A; Institute of Molecular Genetics, Russian Academy of Sciences, Moscow, 123182, Russia., Murakami KS; Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, PA, 16802, USA. kum14@psu.edu. |
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| Jazyk: | angličtina |
| Zdroj: | Nature communications [Nat Commun] 2021 Jan 22; Vol. 12 (1), pp. 528. Date of Electronic Publication: 2021 Jan 22. |
| DOI: | 10.1038/s41467-020-20776-y |
| Abstrakt: | Ribosomal RNA (rRNA) is most highly expressed in rapidly growing bacteria and is drastically downregulated under stress conditions by the global transcriptional regulator DksA and the alarmone ppGpp. Here, we determined cryo-electron microscopy structures of the Escherichia coli RNA polymerase (RNAP) σ 70 holoenzyme during rRNA promoter recognition with and without DksA/ppGpp. RNAP contacts the UP element using dimerized α subunit carboxyl-terminal domains and scrunches the template DNA with the σ finger and β' lid to select the transcription start site favorable for rapid promoter escape. Promoter binding induces conformational change of σ domain 2 that opens a gate for DNA loading and ejects σ |
| Databáze: | MEDLINE |
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